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Progress in Chemistry 2010, Vol. 22 Issue (06): 1203-1211 Previous Articles   Next Articles

• Invited Article •

Expanding Protein Functionalities by Rational Design of Artificial Metal-binding Sites

Lin Yingwu*   

  1. (School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China)
  • Received: Revised: Online: Published:
  • Contact: Lin Yingwu E-mail:ywlin@illinois.edu
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Metal ions play crucial roles in mediating the structure and function of metalloproteins in biological systems. This review summarized the progress of using rational design of artificial metal-binding sites to expand the functional diversity of proteins, which includes designing artificial metal-binding sites within protein scaffolds by exploring potential metal-binding sites, redesigning existing metal-binding sites, or designing new metal-binding sites, and on the protein surfaces to achieve structural and functional conversions, study interactions with nanomaterials, or perform proteins self-assembly. These progresses greatly enriched our knowledge of the structure-function relationships of metalloproteins, and also endowed us the ability of controlling and utilizing a protein of interest.

Contents
1 Introduction
2 Design of Metal-binding Sites within Protein Scaffolds
2.1 Exploring Potential Metal-binding Sites
2.2 Redesigning Existing Metal-binding Sites
2.3 Designing New Metal-binding Sites
3 Design of Metal-binding Sites on Protein Surfaces
3.1 Structural and Functional Conversions
3.2 Interactions with Nanomaterials
3.3 Proteins Self-assembly
4 Conclusions and Outlook

Key words: metal-binding site, molecular design, structure, function

CLC Number: 

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